Iminosuccinic acid

Iminosuccinic acid
Names
	IUPAC name 2-Iminobutanedioic acid
	Other names Iminoaspartic acid; 2-iminobutanedioic acid, iminosuccinate, alpha-iminosuccinate, iminosuccinic acid
Identifiers
CAS Number	79067-61-1;
3D model (JSmol)	Interactive image;
ChEBI	CHEBI:50616;
ChemSpider	13628208;
KEGG	C05840;
PubChem CID	796;
UNII	QHW8YF5XND ;
CompTox Dashboard (EPA)	DTXSID30868498 ;
	InChI InChI=1S/C4H5NO4/c5-2(4(8)9)1-3(6)7/h5H,1H2,(H,6,7)(H,8,9) Key: NMUOATVLLQEYHI-UHFFFAOYSA-N; InChI=1/C4H5NO4/c5-2(4(8)9)1-3(6)7/h5H,1H2,(H,6,7)(H,8,9) Key: NMUOATVLLQEYHI-UHFFFAOYAF;
	SMILES C(C(=N)C(=O)O)C(=O)O;
Properties
Chemical formula	C4H5NO4
Molar mass	131.087 g·mol−1
	Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). Infobox references

Iminoaspartic acid (also known as iminosuccinate or iminoaspartate) is a dicarboxylic acid used in the biosynthesis of nicotinic acid and nicotinamide adenine dinucleotide.

Biosynthesis

The enzyme L-aspartate oxidase oxidises L-aspartic acid:^[1]

aspartic acid

O₂

H₂O₂

Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left

O₂

H₂O₂

iminosuccinic acid

Subsequent conversions

In Escherichia coli another enzyme, quinolinate synthase, takes iminosuccinic acid with dihydroxyacetone phosphate to form quinolinic acid.^[2]

dihydroxyacetone phosphate

+

iminosuccinic acid

2 H₂O

Reversible left-right reaction arrow with minor forward product(s) to top right and minor reverse substrate(s) from bottom right

2 H₂O

quinolinic acid

+ H₃PO₄

This iron-sulfur protein requires a [4Fe-4S] cluster for activity. The quinolinic acid can be converted to nicotinic acid or incorporated into nicotinamide adenine dinucleotide.^[3]

References

↑ Nasu S, Wicks FD, Gholson RK (1982). "L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase". J. Biol. Chem. 257 (2): 626–32. doi:10.1016/S0021-9258(19)68239-6. PMID 7033218.
↑ Ollagnier-de Choudens, S., Loiseau, L., Sanakis, Y., Barras, F. and Fontecave, M. (2005). "Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis" (PDF). FEBS Lett. 579 (17): 3737–3743. doi:10.1016/j.febslet.2005.05.065. PMID 15967443.{{cite journal}}: CS1 maint: multiple names: authors list (link)
↑ Rousset C, Fontecave M, Ollagnier de Choudens S (August 2008). "The [4Fe-4S] cluster of quinolinate synthase from Escherichia coli: investigation of cluster ligands". FEBS Letters. 582 (19): 2937–44. Bibcode:2008FEBSL.582.2937R. doi:10.1016/j.febslet.2008.07.032. PMID 18674537.

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[1] Nasu S, Wicks FD, Gholson RK (1982). "L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase". J. Biol. Chem. 257 (2): 626–32. doi:10.1016/S0021-9258(19)68239-6. PMID 7033218.

[2] Ollagnier-de Choudens, S., Loiseau, L., Sanakis, Y., Barras, F. and Fontecave, M. (2005). "Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis" (PDF). FEBS Lett. 579 (17): 3737–3743. doi:10.1016/j.febslet.2005.05.065. PMID 15967443.{{cite journal}}: CS1 maint: multiple names: authors list (link)

[3] Rousset C, Fontecave M, Ollagnier de Choudens S (August 2008). "The [4Fe-4S] cluster of quinolinate synthase from Escherichia coli: investigation of cluster ligands". FEBS Letters. 582 (19): 2937–44. Bibcode:2008FEBSL.582.2937R. doi:10.1016/j.febslet.2008.07.032. PMID 18674537.

[1]

[2]

[3]

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Biosynthesis

Subsequent conversions

References